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Progress over the first decade of CASP experiments
Author(s) -
Kryshtafovych Andriy,
Venclovas Česlovas,
Fidelis Krzysztof,
Moult John
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20740
Subject(s) - casp , protein structure prediction , computer science , data science , biology , protein structure , biochemistry
CASP has now completed a decade of monitoring the state of the art in protein structure prediction. The quality of structure models produced in the latest experiment, CASP6, has been compared with that in earlier CASPs. Significant although modest progress has again been made in the fold recognition regime, and cumulatively, progress in this area is impressive. Models of previously unknown folds again appear to have modestly improved, and several mixed α/β structures have been modeled in a topologically correct manner. Progress remains hard to detect in high sequence identity comparative modeling, but server performance in this area has moved forward. Proteins 2005;61:225–236. © 2005 Wiley‐Liss, Inc.